Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins

Increase in Surface Hydrophobicity of the Cataract-Associated P23T Mutant of Human γD-Crystallin Is Responsible for Its Dramatically Lower, Retrograde Solubility

(2010) Ajay Pande et al.   BIOCHEMISTRY

Cataract-associated mutant E107A of human  D-crystallin shows increased attraction to  -crystallin and enhanced light scattering

(2010) P. R. Banerjee et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Structure of the Cataract-Causing P23T Mutant of Human γD-Crystallin Exhibits Distinctive Local Conformational and Dynamic Changes†,‡

(2009) Jinwon Jung et al.   BIOCHEMISTRY

Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins

(2009) Hassane S. Mchaourab et al.   BIOCHEMISTRY

Lens aging: Effects of crystallins

(2009) K. Krishna Sharma et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Hydrophobic Core Mutations Associated with Cataract Development in Mice Destabilize Human γD-Crystallin

(2009) Kate L. Moreau et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structure and Orientation of T4 Lysozyme Bound to the Small Heat Shock Protein α-Crystallin

(2007) Derek P. Claxton et al.   JOURNAL OF MOLECULAR BIOLOGY